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Identification
HMDB Protein ID HMDBP07806
Secondary Accession Numbers
  • 13515
Name Matrix metalloproteinase-17
Synonyms
  1. MMP-17
  2. MT-MMP 4
  3. MT4-MMP
  4. MT4MMP
  5. MTMMP4
  6. Membrane-type matrix metalloproteinase 4
  7. Membrane-type-4 matrix metalloproteinase
Gene Name MMP17
Protein Type Unknown
Biological Properties
General Function Involved in metalloendopeptidase activity
Specific Function Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin
Pathways Not Available
Reactions Not Available
GO Classification
Component
extracellular region part
extracellular matrix
Function
endopeptidase activity
ion binding
cation binding
metal ion binding
binding
catalytic activity
hydrolase activity
transition metal ion binding
zinc ion binding
metalloendopeptidase activity
peptidase activity
peptidase activity, acting on l-amino acid peptides
metallopeptidase activity
calcium ion binding
Process
metabolic process
macromolecule metabolic process
protein metabolic process
proteolysis
Cellular Location
  1. Lipid-anchor
  2. GPI-anchor
  3. Secreted
  4. extracellular space
  5. Extracellular side
  6. extracellular matrix
  7. Isoform Long:Cell membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 12q24.3
SNPs MMP17
Gene Sequence
>1812 bp
ATGCGGCGCCGCGCAGCCCGGGGACCCGGCCCGCCGCCCCCAGGGCCCGGACTCTCGCGG
CTGCCGCTGCCGCTGCTGCTGCTGCTGGCGCTGGGGACCCGCGGGGGCTGCGCCGCGCCC
GCACCCGCGCCGCGCGCCGAGGACCTCAGCCTGGGAGTGGAGTGGCTAAGCAGGTTCGGT
TACCTGCCCCCGGCTGACCCCACAACAGGGCAGCTGCAGACGCAAGAGGAGCTGTCTAAG
GCCATCACAGCCATGCAGCAGTTTGGTGGCCTGGAGGCCACCGGCATCCTGGACGAGGCC
ACCCTGGCCCTGATGAAAACCCCACGCTGCTCCCTGCCAGACCTCCCTGTCCTGACCCAG
GCTCGCAGGAGACGCCAGGCTCCAGCCCCCACCAAGTGGAACAAGAGGAACCTGTCGTGG
AGGGTCCGGACGTTCCCACGGGACTCACCACTGGGGCACGACACGGTGCGTGCACTCATG
TACTACGCCCTCAAGGTCTGGAGCGACATTGCGCCCCTGAACTTCCACGAGGTGGCGGGC
AGCGCCGCCGACATCCAGATCGACTTCTCCAAGGCCGACCATAACGACGGCTACCCCTTC
GACGGCCCCGGCGGCACCGTGGCCCACGCCTTCTTCCCCGGCCACCACCACACCGCCGGG
GACACCCACTTTGACGATGACGAGGCCTGGACCTTCCGCTCCTCGGATGCCCACGGGATG
GACCTGTTTGCAGTGGCTGTCCACGAGTTTGGCCACGCCATTGGGTTAAGCCATGTGGCC
GCTGCACACTCCATCATGCGGCCGTACTACCAGGGCCCGGTGGGTGACCCGCTGCGCTAC
GGGCTCCCCTACGAGGACAAGGTGCGCGTCTGGCAGCTGTACGGTGTGCGGGAGTCTGTG
TCTCCCACGGCGCAGCCCGAGGAGCCTCCCCTGCTGCCGGAGCCCCCAGACAACCGGTCC
AGCGCCCCGCCCAGGAAGGACGTGCCCCACAGATGCAGCACTCACTTTGACGCGGTGGCC
CAGATCCGGGGTGAAGCTTTCTTCTTCAAAGGCAAGTACTTCTGGCGGCTGACGCGGGAC
CGGCACCTGGTGTCCCTGCAGCCGGCACAGATGCACCGCTTCTGGCGGGGCCTGCCGCTG
CACCTGGACAGCGTGGACGCCGTGTACGAGCGCACCAGCGACCACAAGATCGTCTTCTTT
AAAGGAGACAGGTACTGGGTGTTCAAGGACAATAACGTAGAGGAAGGATACCCGCGCCCC
GTCTCCGACTTCAGCCTCCCGCCTGGCGGCATCGACGCTGCCTTCTCCTGGGCCCACAAT
GACAGGACTTATTTCTTTAAGGACCAGCTGTACTGGCGCTACGATGACCACACGAGGCAC
ATGGACCCCGGCTACCCCGCCCAGAGCCCCCTGTGGAGGGGTGTCCCCAGCACGCTGGAC
GACGCCATGCGCTGGTCCGACGGTGCCTCCTACTTCTTCCGTGGCCAGGAGTACTGGAAA
GTGCTGGATGGCGAGCTGGAGGTGGCACCCGGGTACCCACAGTCCACGGCCCGGGACTGG
CTGGTGTGTGGAGACTCACAGGCCGATGGATCTGTGGCTGCGGGCGTGGACGCGGCAGAG
GGGCCCCGCGCCCCTCCAGGACAACATGACCAGAGCCGCTCGGAGGACGGTTACGAGGTC
TGCTCATGCACCTCTGGGGCATCCTCTCCCCCGGGGGCCCCAGGCCCACTGGTGGCTGCC
ACCATGCTGCTGCTGCTGCCGCCACTGTCACCAGGCGCCCTGTGGACAGCGGCCCAGGCC
CTGACGCTATGA
Protein Properties
Number of Residues 603
Molecular Weight 66652.2
Theoretical pI 6.55
Pfam Domain Function
Signals
  • 1-35
Transmembrane Regions
  • None
Protein Sequence
>Matrix metalloproteinase-17
MRRRAARGPGPPPPGPGLSRLPLPLLLLLALGTRGGCAAPAPAPRAEDLSLGVEWLSRFG
YLPPADPTTGQLQTQEELSKAITAMQQFGGLEATGILDEATLALMKTPRCSLPDLPVLTQ
ARRRRQAPAPTKWNKRNLSWRVRTFPRDSPLGHDTVRALMYYALKVWSDIAPLNFHEVAG
SAADIQIDFSKADHNDGYPFDGPGGTVAHAFFPGHHHTAGDTHFDDDEAWTFRSSDAHGM
DLFAVAVHEFGHAIGLSHVAAAHSIMRPYYQGPVGDPLRYGLPYEDKVRVWQLYGVRESV
SPTAQPEEPPLLPEPPDNRSSAPPRKDVPHRCSTHFDAVAQIRGEAFFFKGKYFWRLTRD
RHLVSLQPAQMHRFWRGLPLHLDSVDAVYERTSDHKIVFFKGDRYWVFKDNNVEEGYPRP
VSDFSLPPGGIDAAFSWAHNDRTYFFKDQLYWRYDDHTRHMDPGYPAQSPLWRGVPSTLD
DAMRWSDGASYFFRGQEYWKVLDGELEVAPGYPQSTARDWLVCGDSQADGSVAAGVDAAE
GPRAPPGQHDQSRSEDGYEVCSCTSGASSPPGAPGPLVAATMLLLLPPLSPGALWTAAQA
LTL
GenBank ID Protein 112382270
UniProtKB/Swiss-Prot ID Q9ULZ9
UniProtKB/Swiss-Prot Entry Name MMP17_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_016155.4
GeneCard ID MMP17
GenAtlas ID MMP17
HGNC ID HGNC:7163
References
General References
  1. Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed:16541075 ]
  2. Kajita M, Kinoh H, Ito N, Takamura A, Itoh Y, Okada A, Sato H, Seiki M: Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts. FEBS Lett. 1999 Sep 3;457(3):353-6. [PubMed:10471807 ]
  3. Puente XS, Pendas AM, Llano E, Velasco G, Lopez-Otin C: Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma. Cancer Res. 1996 Mar 1;56(5):944-9. [PubMed:8640782 ]
  4. Wang Y, Johnson AR, Ye QZ, Dyer RD: Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain. J Biol Chem. 1999 Nov 12;274(46):33043-9. [PubMed:10551873 ]
  5. Itoh Y, Kajita M, Kinoh H, Mori H, Okada A, Seiki M: Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase. J Biol Chem. 1999 Nov 26;274(48):34260-6. [PubMed:10567400 ]
  6. Kolkenbrock H, Essers L, Ulbrich N, Will H: Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase. Biol Chem. 1999 Sep;380(9):1103-8. [PubMed:10543448 ]